3gzu

<StructureSection load='3gzu' size='340' side='right' caption='[[3gzu]], [[Resolution|resolution]] 3.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[3gzu]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhesus_rotavirus Rhesus rotavirus] and [http://en.wikipedia.org/wiki/Rotavirus_a Rotavirus a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GZU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GZU FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>

<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gzt|3gzt]]</td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gzu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gzu RCSB], [http://www.ebi.ac.uk/pdbsum/3gzu PDBsum]</span></td></tr>

<table>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gz/3gzu_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Rotaviruses, major causes of childhood gastroenteritis, are nonenveloped, icosahedral particles with double-strand RNA genomes. By the use of electron cryomicroscopy and single-particle reconstruction, we have visualized a rotavirus particle comprising the inner capsid coated with the trimeric outer-layer protein, VP7, at a resolution (4 A) comparable with that of X-ray crystallography. We have traced the VP7 polypeptide chain, including parts not seen in its X-ray crystal structure. The 3 well-ordered, 30-residue, N-terminal "arms" of each VP7 trimer grip the underlying trimer of VP6, an inner-capsid protein. Structural differences between free and particle-bound VP7 and between free and VP7-coated inner capsids may regulate mRNA transcription and release. The Ca(2+)-stabilized VP7 intratrimer contact region, which presents important neutralizing epitopes, is unaltered upon capsid binding.

Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM.,Chen JZ, Settembre EC, Aoki ST, Zhang X, Bellamy AR, Dormitzer PR, Harrison SC, Grigorieff N Proc Natl Acad Sci U S A. 2009 Jun 30;106(26):10644-8. Epub 2009 Jun 1. PMID:19487668<ref>PMID:19487668</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

*[[Virus coat protein|Virus coat protein]]

</StructureSection>

[[Category: Rhesus rotavirus]]

[[Category: Rotavirus a]]

[[Category: Chen, J Z.]]

[[Category: Grigorieff, N.]]

[[Category: Harrison, S C.]]

[[Category: Settembre, E C.]]

[[Category: 7rp]]

[[Category: Vp7]]